K
Keith Rose
Researcher at University of Geneva
Publications - 95
Citations - 3296
Keith Rose is an academic researcher from University of Geneva. The author has contributed to research in topics: Peptide & Peptide sequence. The author has an hindex of 33, co-authored 95 publications receiving 3250 citations. Previous affiliations of Keith Rose include Cooperative Research Centre & University of Manitoba.
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Facile synthesis of homogeneous artificial proteins
TL;DR: One of the compounds made, the covalent structure of which was defined by electrospray mass spectrometry, would seem to be the largest artificial protein ever made, in pure form in good yield, by controlled total synthesis.
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Construction of protein analogues by site-specific condensation of unprotected fragments
TL;DR: This method represents a new, reasonably general route for the construction of large protein chimeras of precisely controlled structure by allowing such oxidized peptides to react with others that have had a hydrazide derivative attached to the C-terminus by reversed proteolysis.
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A Totally Synthetic Polyoxime Malaria Vaccine Containing Plasmodium falciparum B Cell and Universal T Cell Epitopes Elicits Immune Responses in Volunteers of Diverse HLA Types
Elizabeth Nardin,J. Mauricio Calvo-Calle,Giane A. Oliveira,Ruth S. Nussenzweig,Martin Schneider,Jean-Marie Tiercy,Louis Loutan,Denis F. Hochstrasser,Keith Rose +8 more
TL;DR: The excellent correlation of T*-specific cellular responses with high anti-repeat Ab titers suggests that the T* epitope functioned as a universal Th cell epitope, as predicted by previous peptide/HLA binding assays and by immunogenicity studies in mice of diverse H-2 haplotypes.
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Development of an isotope dilution assay for precise determination of insulin, C-peptide, and proinsulin levels in non-diabetic and type II diabetic individuals with comparison to immunoassay
Alistair D. Kippen,Fabrice Cerini,Laszlo Vadas,Reto Stöcklin,Lan Vu,Robin E. Offord,Keith Rose +6 more
TL;DR: Stable isotope dilution assay was shown to give direct, positive identification of the target protein with unrivaled accuracy, avoiding many of the problems associated with present methodology for protein determination.
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Purification and characterization of human interleukin‐1β expressed in recombinant Escherichia coli
Paul T. Wingfield,Mark A. Payton,Jean Tavernier,Marjory Barnes,Alan Shaw,Keith Rose,M G Simona,Stephen Demczuk,Karen Williamson,Jean-Michel Dayer +9 more
TL;DR: The high-level expression of human interleukin-1β in Escherichia coli is described and the isolated protein, shown to be homogeneous by several analytical methods, has been characterized by amino acid analysis, N- and C-terminal sequence analysis and analytical centrifugation.